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    #4114 at 2020-05-05 19:24:20 (UTC+1)

    https://pubmed.ncbi.nlm.nih.gov/16115318/
    https://www.thelancet.com/journals/lancet/article/PIIS0140-6736(20)30251-8/fulltext
    When the protein sequence of the SARS-CoV-2 receptor binding site was analyzed, an interesting result was found. While SARS-CoV-2 is overall more similar to bat coronaviruses, the receptor binding site was more similar to SARS-CoV.
    https://www.cell.com/cell/fulltext/S0092-8674(20)30262-2?_returnURL=https%3A%2F%2Flinkinghub.elsevier.com%2Fretrieve%2Fpii%2FS0092867420302622%3Fshowall%3Dtrue
    Both SARS-CoV-2 and SARS-CoV use the same host cell receptor. It also found that, for both viruses, the viral proteins used for host cell entry bind to the receptor with the same tightness (affinity).
    Knowledge is power.
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    https://pubmed.ncbi.nlm.nih.gov/16115318/ https://www.thelancet.com/journals/lancet/article/PIIS0140-6736(20)30251-8/fulltext When the protein sequence of the SARS-CoV-2 receptor binding site was analyzed, an interesting result was found. While SARS-CoV-2 is overall more similar to bat coronaviruses, the receptor binding site was more similar to SARS-CoV. https://www.cell.com/cell/fulltext/S0092-8674(20)30262-2?_returnURL=https%3A%2F%2Flinkinghub.elsevier.com%2Fretrieve%2Fpii%2FS0092867420302622%3Fshowall%3Dtrue Both SARS-CoV-2 and SARS-CoV use the same host cell receptor. It also found that, for both viruses, the viral proteins used for host cell entry bind to the receptor with the same tightness (affinity). Knowledge is power. PUBMED: Virol J . 2005 Aug 22;2:69. doi: 10.1186/1743-422X-2-69. Chloroquine Is a Potent Inhibitor of SARS Coronavirus Infection and Spread Martin J Vincent 1, Eric Bergeron, Suzanne Benjannet, Bobbie R Erickson, Pierre E Rollin, Thomas G Ksiazek, Nabil G Seidah, Stuart T Nichol Affiliations expand PMID: 16115318 PMCID: PMC1232869 DOI: 10.1186/1743-422X-2-69 Abstract Background: Severe acute respiratory syndrome (SARS) is caused by a newly discovered coronavirus (SARS-CoV). No effective prophylactic or post-exposure therapy is currently available. https://archive.fo/dmhwp THE LANCET: VOLUME 395, ISSUE 10224, P565-574, FEBRUARY 22, 2020 Genomic characterisation and epidemiology of 2019 novel coronavirus: implications for virus origins and receptor binding Prof Roujian Lu, MSc *• Xiang Zhao, MD *• Juan Li, PhD *• Peihua Niu, PhD *• Bo Yang, MSc *• Honglong Wu, MSc *• et al. Published:January 30, 2020•DOI:https://doi.org/10.1016/S0140-6736(20)30251-8 Summary Background In late December, 2019, patients presenting with viral pneumonia due to an unidentified microbial agent were reported in Wuhan, China. A novel coronavirus was subsequently identified as the causative pathogen, provisionally named 2019 novel coronavirus (2019-nCoV). As of Jan 26, 2020, more than 2000 cases of 2019-nCoV infection have been confirmed, most of which involved people living in or visiting Wuhan, and human-to-human transmission has been confirmed. https://archive.fo/CKpNB CELL.COM: VOLUME 181, ISSUE 2, P281-292.E6, APRIL 16, 2020 Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein Alexandra C. Walls 5 • Young-Jun Park 5 • M. Alejandra Tortorici • Abigail Wall • Andrew T. McGuire • David Veesler 6 Open Access•Published:March 09, 2020•DOI:https://doi.org/10.1016/j.cell.2020.02.058• PlumX Metrics Highlights • SARS-CoV-2 uses ACE2 to enter target cells • SARS-CoV-2 and SARS-CoV bind with similar affinities to ACE2 • Structures of SARS-CoV-2 spike glycoprotein in two conformations • SARS-CoV polyclonal antibodies inhibit SARS-CoV-2 spike-mediated entry into cells Summary The emergence of SARS-CoV-2 has resulted in >90,000 infections and >3,000 deaths. Coronavirus spike (S) glycoproteins promote entry into cells and are the main target of antibodies. We show that SARS-CoV-2 S uses ACE2 to enter cells and that the receptor-binding domains of SARS-CoV-2 S and SARS-CoV S bind with similar affinities to human ACE2, correlating with the efficient spread of SARS-CoV-2 among humans. We found that the SARS-CoV-2 S glycoprotein harbors a furin cleavage site at the boundary between the S1/S2 subunits, which is processed during biogenesis and sets this virus apart from SARS-CoV and SARS-related CoVs. We determined cryo-EM structures of the SARS-CoV-2 S ectodomain trimer, providing a blueprint for the design of vaccines and inhibitors of viral entry. Finally, we demonstrate that SARS-CoV S murine polyclonal antibodies potently inhibited SARS-CoV-2 S mediated entry into cells, indicating that cross-neutralizing antibodies targeting conserved S epitopes can be elicited upon vaccination. https://archive.fo/pVKAV

    Patents by Inventor Anthony S. Fauci Anthony S. Fauci has filed for patents to protect the following inventions. This listing includes patent applications that are pending as well as patents that have already been granted by the United States Patent and Trademark Office (USPTO). https://patents.justia.com/inventor/anthony-s-fauci Use of antagonists of the interaction between HIV GP120 and ?4?7 integrin Patent number: 9896509 USE OF ANTAGONISTS OF THE INTERACTION BETWEEN HIV GP120 AND A4B7 INTEGRIN Publication number: 20160333097 USE OF ANTAGONISTS OF THE INTERACTION BETWEEN HIV GP120 AND A4B7 INTEGRIN Publication number: 20160075786 IMMUNOCONJUGATES COMPRISING CD4 AND IMMUNOGLOBIN MOLECULES FOR THE TREATMENT OF HIV INFECTION Publication number: 20090285815 Fusion protein including of CD4 Patent number: 7368114 HIV related peptides Patent number: 6911527 Efficient inhibition of hiv-1 viral entry through a novel fusion protein including of cd4 Publication number: 20040265306 Immunologic enhancement with intermittent interleukin-2 therapy Patent number: 5696079 Immunologic enhancement with intermittent interleukin-2 therapy Patent number: 6190656 Immunologic enhancement with intermittent interleukin-2 therapy Patent number: 6548055 Here is Fauci's latest patent. Use of antagonists of the interaction between HIV GP120 and ?4?7 integrin Patent number: 9896509 Abstract: Methods are provided for the treatment of a HIV infection. The methods can include administering to a subject with an HIV infection a therapeutically effective amount of an agent that interferes with the interaction of gp120 and ?4 integrin, such as a ?4?1 or ?4?7 integrin antagonist, thereby treating the HIV infection. In several examples, the ?4 integrin antagonist is a monoclonal antibody that specifically binds to a ?4, ?1 or ?7 integrin subunit or a cyclic hexapeptide with the amino acid sequence of CWLDVC. Methods are also provided to reduce HIV replication or infection. The methods include contacting a cell with an effective amount of an agent that interferes with the interaction of gp120 and ?4 integrin, such as a ?4?1 or ?4?7 integrin antagonist. Moreover, methods are provided for determining if an agent is useful to treat HIV. Type: Grant Filed: August 3, 2016 Date of Patent: February 20, 2018 Assignee: The United States of America, as Represented by the Secretary, Department of Health and Human Services Inventors: James Arthos, Diana Goode, Claudia Cicala, Anthony S. Fauci SCREENSHOT: https://postimg.cc/zb2dBhj2